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Nat Struct Mol Biol. 2006 Mar;13(3):250-5. Epub 2006 Feb 5.

Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo.

Author information

1
Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, USA.

Erratum in

  • Nat Struct Mol Biol. 2006 May;13(5):465.

Abstract

H1 linker histones stabilize the nucleosome, limit nucleosome mobility and facilitate the condensation of metazoan chromatin. Here, we have combined systematic mutagenesis, measurement of in vivo binding by photobleaching microscopy, and structural modeling to determine the binding geometry of the globular domain of the H1(0) linker histone variant within the nucleosome in unperturbed, native chromatin in vivo. We demonstrate the existence of two distinct DNA-binding sites within the globular domain that are formed by spatial clustering of multiple residues. The globular domain is positioned via interaction of one binding site with the major groove near the nucleosome dyad. The second site interacts with linker DNA adjacent to the nucleosome core. Multiple residues bind cooperatively to form a highly specific chromatosome structure that provides a mechanism by which individual domains of linker histones interact to facilitate chromatin condensation.

PMID:
16462749
PMCID:
PMC1868459
DOI:
10.1038/nsmb1050
[Indexed for MEDLINE]
Free PMC Article

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